1996
DOI: 10.1016/s0091-6749(96)70199-9
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Allergy to the heat-labile proteins α-lactalbumin and β-lactoglobulin in mare’s milk

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Cited by 41 publications
(12 citation statements)
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“…Indeed, when we performed the alternate "nonreducing/nonboiling" procedure, we observed more IgE-binding polypeptides for sera Hu and Kr in bumblebee venom, an observation which underlines the fact that the Laemmli procedure can lead to denaturation of conformational epitopes. Comparable observations have been reported by Gall et al (22), who found that boiling of mare's milk led to loss of IgE-binding capacity, and by Wiithrich et al (23), who observed that the activity of celery extract in skin tests and RAST was strongly reduced after boiling. Immunoblotting of serum Kr, on venom proteins separated by Laemmli's procedure for SDS-PAGE, showed IgE binding to blotted European bumblebee venom 17-kDa protein, but not to American bumblebee venom.…”
Section: Discussionsupporting
confidence: 77%
“…Indeed, when we performed the alternate "nonreducing/nonboiling" procedure, we observed more IgE-binding polypeptides for sera Hu and Kr in bumblebee venom, an observation which underlines the fact that the Laemmli procedure can lead to denaturation of conformational epitopes. Comparable observations have been reported by Gall et al (22), who found that boiling of mare's milk led to loss of IgE-binding capacity, and by Wiithrich et al (23), who observed that the activity of celery extract in skin tests and RAST was strongly reduced after boiling. Immunoblotting of serum Kr, on venom proteins separated by Laemmli's procedure for SDS-PAGE, showed IgE binding to blotted European bumblebee venom 17-kDa protein, but not to American bumblebee venom.…”
Section: Discussionsupporting
confidence: 77%
“…With regard to the potential allergenic role of equid milk proteins, Gall, Kalveram, Sick, and Sterry (1996) reported on the IgEmediated horse milk allergy in one adult, most likely caused by heat-labile proteins a-lactalbumin and b-lactoglobulin in milk. For details on chemistry, structure and nutritional significance of horse milk proteins, the reader is referred to the review by Uniacke-Lowe et al (2010).…”
Section: Nitrogenous Componentsmentioning
confidence: 99%
“…IgE antibodies to animal-derived proteins are known to occur in about 2% of the population and in about 40% of atopic individuals making any animal an important source of inhalant allergens (Spitzauer, 1999). Gall, Kalveram, Sick, and Sterry (1996) demonstrated the existence of an IgE-mediated equine milk allergy in one patient, caused by low molecular mass heat-labile proteins, most likely a-La and b-Lg, without cross-reaction to the corresponding whey proteins from bovine milk. Presumably, the above cases are not isolated incidents and as the consumption of equine milk and its products increases, it is likely that further cases will be reported.…”
Section: Cross Reactivity Of Proteinsmentioning
confidence: 99%